| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8399224 | Mitochondrion | 2015 | 8 Pages |
Abstract
The biogenesis of mitochondrial respiratory chain components is complex. Mammalian complex I (NADH:ubiquinone oxidoreductase) contains 44 different subunits, an FMN and seven iron-sulfur centers. Its assembly involves at least twelve additional proteins, called assembly factors. One of these is FOXRED1, a 486-amino acid FAD-dependent oxidoreductase. FOXRED1 is a member of the d-amino acid oxidase (DAO) family. A structural model of FOXRED1 reveals a large substrate-binding cavity and a putative oxygen-binding site. These features strongly suggest that FOXRED1 is catalytically active as an oxidoreductase. A metabolic role for FOXRED1 in the biogenesis of complex I should be considered.
Keywords
cpsmethylenetetrahydrofolate dehydrogenaseDMGOsarcosine dehydrogenasePCK2Dimethylglycine dehydrogenaseTMEMSCOMDHSHMTRMSDd-amino acid oxidaseMitochondrial DNANADH:ubiquinone oxidoreductaseOxidaseMitochondrial diseaseHADHADAOmtDNAserine hydroxymethyltransferaseLeigh syndromephosphoenolpyruvate carboxykinaseFlavoproteinStructural modelmalate dehydrogenaseroot mean square deviationTransmembrane protein
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Authors
Bernard D. Lemire,